6LKC

Crystal structure of PfaD from Shewanella piezotolerans in complex with FMN

Summary for 6LKC

• Entry DOI: 10.2210/pdb6lkc/pdb
• Descriptor: Polyunsaturated fatty acid synthase PfaD, FLAVIN MONONUCLEOTIDE, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: fatty acid synthesis, pks, enoyl reductase, biosynthetic protein
• Biological source: Shewanella piezotolerans (strain WP3 / JCM 13877)
• Total number of polymer chains: 2
• Total formula weight: 130107.45

Authors

Zhang, M.L.,Li, Q.,Meng, S.S.,Guo, L.J.,He, L.,Huang, J.Z.,Li, L.,Zhang, H.D. (deposition date: 2019-12-19, release date: 2020-12-23, Last modification date: 2023-11-22)

Primary citation

Zhang, M.,Zhang, H.,Li, Q.,Gao, Y.,Guo, L.,He, L.,Zang, S.,Guo, X.,Huang, J.,Li, L.
Structural Insights into the Trans -Acting Enoyl Reductase in the Biosynthesis of Long-Chain Polyunsaturated Fatty Acids in Shewanella piezotolerans .
J.Agric.Food Chem., 69:2316-2324, 2021

PubMed Abstract: Two long-chain polyunsaturated fatty acids (LC-PUFAs), eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), play vital roles in human health. Similarly, two biosynthetic pathways, based on desaturase/elongase and polyketide synthase, have been implicated in the synthesis of microbial LC-PUFA. Up to now, only several microalgae, no bacteria, have been used in the commercial production of oils rich in DHA and/or EPA. Fully understanding the enzymatic mechanism in the biosynthesis of LC-PUFA would contribute significantly to produce EPA and/or DHA by the bacteria. In this study, we report a 1.998 Å-resolution crystal structure of -acting enoyl reductase (ER), SpPfaD, from . The SpPfaD model consists of one homodimer in the asymmetric unit, and each subunit contains three domains. These include an N-terminal, a central domain forming a classic TIM barrel with a single FMN cofactor molecule bound atop the barrel, and a C-terminal domain with a lid above the TIM barrel. Furthermore, we docked oxidized nicotinamide adenine dinucleotide phosphate (NADP) and an inhibitor 2-(4-(2-((3-(5-(pyridin-2-ylthio)thiazol-2-yl)ureido)methyl)-1-imidazole-4-yl)phenoxy)acetic acid (TUI) molecule into the active site and analyzed the inhibition and catalytic mechanisms of the enoyl reductase SpPfaD. To the best of our knowledge, this is the first crystal structure of -ER in the biosynthesis of bacterial polyketides.

PubMed: 33587627
DOI: 10.1021/acs.jafc.0c07386

Experimental method

X-RAY DIFFRACTION (1.998 Å)